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  • Title: Tetrafibricin: a nonpeptidic fibrinogen receptor inhibitor from Streptomyces neyagawaensis (I). Its GPIIb/IIIa blockage on solid phase binding assay.
    Author: Satoh T, Yamashita Y, Kamiyama T, Watanabe J, Steiner B, Hadváry P, Arisawa M.
    Journal: Thromb Res; 1993 Dec 01; 72(5):389-400. PubMed ID: 8303682.
    Abstract:
    Tetrafibricin is a novel nonpeptidic fibrinogen receptor inhibitor isolated from Streptomyces neyagawaensis NR0577. Its competitive and selective fibrinogen receptor blockage was demonstrated in this study. Tetrafibricin competitively inhibited (Ki = 9.9 nM) the binding of biotinylated fibrinogen to purified active glycoprotein (GP) IIb/IIIa immobilized on plastic plate. When RGDS and tetrafibricin were added in combination, the inhibition was additive. The binding of other RGD-containing proteins, fibronectin and von Willebrand factor, to active GPIIb/IIIa were also completely inhibited by tetrafibricin. The fact that tetrafibricin did not inhibit the binding of von Willebrand factor to GPIb/IX indicates the specific blockage of tetrafibricin for GPIIb/IIIa. Fibrinogen receptor inhibition of tetrafibricin was also confirmed by its ability to inhibit 125I-fibrinogen binding to platelets stimulated with ADP. Because of its competitiveness and specificity, tetrafibricin can be used in a new structural model for the design of fibrinogen receptor inhibitors.
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